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• W2045647626 abstract "F(1)-ATPase is a rotary molecular motor in which the central gamma subunit rotates inside a cylinder made of alpha(3)beta(3) subunits. To clarify how ATP hydrolysis in three catalytic sites cooperate to drive rotation, we measured the site occupancy, the number of catalytic sites occupied by a nucleotide, while assessing the hydrolysis activity under identical conditions. The results show hitherto unsettled timings of ADP and phosphate releases: starting with ATP binding to a catalytic site at an ATP-waiting gamma angle defined as 0 degrees , phosphate is released at approximately 200 degrees , and ADP is released during quick rotation between 240 degrees and 320 degrees that is initiated by binding of a third ATP. The site occupancy remains two except for a brief moment after the ATP binding, but the third vacant site can bind a medium nucleotide weakly." @default.
• W2045647626 created "2016-06-24" @default.
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• W2045647626 date "2010-04-01" @default.
• W2045647626 modified "2023-09-24" @default.
• W2045647626 title "Chemo-Mechanical Coupling in F1-ATPase Revealed by Catalytic Site Occupancy during Catalysis" @default.
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• W2045647626 doi "https://doi.org/10.1016/j.bpj.2009.11.050" @default.
• W2045647626 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/2849061" @default.
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